alpha-glycerophosphoric acid and serine

alpha-glycerophosphoric acid has been researched along with serine in 6 studies

Research

Studies (6)

TimeframeStudies, this research(%)All Research%
pre-19901 (16.67)18.7374
1990's0 (0.00)18.2507
2000's4 (66.67)29.6817
2010's1 (16.67)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Ahmed, SA; Bauerle, R; Kawasaki, H; Miles, EW; Zon, G1
Fan, YX; McPhie, P; Miles, EW2
Herde, P; Marabotti, A; Mozzarelli, A; Schlichting, I; Weyand, M1
Apel, AK; Martín, JF; Rodríguez-García, A; Santos-Beneit, F1
Eisbach, M; Loutchko, D; Mikhailov, AS1

Other Studies

6 other study(ies) available for alpha-glycerophosphoric acid and serine

ArticleYear
Site-specific mutagenesis of the alpha subunit of tryptophan synthase from Salmonella typhimurium. Changing arginine 179 to leucine alters the reciprocal transmission of substrate-induced conformational changes between the alpha and beta 2 subunits.
    The Journal of biological chemistry, 1987, Aug-05, Volume: 262, Issue:22

    Topics: Amino Acid Sequence; Arginine; DNA, Recombinant; Glycerophosphates; Indoles; Kinetics; Leucine; Macromolecular Substances; Mutation; Protein Conformation; Salmonella typhimurium; Serine; Structure-Activity Relationship; Tryptophan Synthase

1987
Regulation of tryptophan synthase by temperature, monovalent cations, and an allosteric ligand. Evidence from Arrhenius plots, absorption spectra, and primary kinetic isotope effects.
    Biochemistry, 2000, Apr-25, Volume: 39, Issue:16

    Topics: Allosteric Regulation; Allosteric Site; Catalysis; Cations, Monovalent; Cesium; Chlorides; Deuterium; Enzyme Activation; Glycerophosphates; Guanidine; Kinetics; Ligands; Protein Conformation; Salmonella typhimurium; Serine; Sodium Chloride; Spectrum Analysis; Temperature; Thermodynamics; Tryptophan Synthase

2000
Thermal repair of tryptophan synthase mutations in a regulatory intersubunit salt bridge. Evidence from arrhenius plots, absorption spectra, and primary kinetic isotope effects.
    The Journal of biological chemistry, 2000, Jul-07, Volume: 275, Issue:27

    Topics: Allosteric Regulation; Bacterial Proteins; Cations, Monovalent; Enzyme Activation; Glycerophosphates; Indoles; Kinetics; Mutation; Protein Conformation; Salmonella typhimurium; Serine; Spectrophotometry; Temperature; Thermodynamics; Tryptophan Synthase

2000
Crystal structure of the beta Ser178--> Pro mutant of tryptophan synthase. A "knock-out" allosteric enzyme.
    The Journal of biological chemistry, 2002, Mar-22, Volume: 277, Issue:12

    Topics: Allosteric Site; Binding Sites; Computer Simulation; Crystallography, X-Ray; Glycerophosphates; Glycine; Hydrogen Bonding; Indoles; Kinetics; Ligands; Models, Chemical; Models, Molecular; Mutation; Proline; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Serine; Tryptophan Synthase

2002
Phosphate and carbon source regulation of two PhoP-dependent glycerophosphodiester phosphodiesterase genes of Streptomyces coelicolor.
    Microbiology (Reading, England), 2009, Volume: 155, Issue:Pt 6

    Topics: Bacterial Proteins; Base Sequence; Carbon; DNA, Bacterial; Gene Expression Regulation, Bacterial; Genes, Bacterial; Glycerophosphates; Inositol; Molecular Sequence Data; Operon; Phosphates; Phosphoric Diester Hydrolases; Promoter Regions, Genetic; Repetitive Sequences, Nucleic Acid; Serine; Streptomyces coelicolor

2009
Stochastic thermodynamics of a chemical nanomachine: The channeling enzyme tryptophan synthase.
    The Journal of chemical physics, 2017, Jan-14, Volume: 146, Issue:2

    Topics: Allosteric Regulation; Entropy; Glycerophosphates; Models, Biological; Molecular Structure; Nanostructures; Protein Subunits; Serine; Stochastic Processes; Thermodynamics; Tryptophan; Tryptophan Synthase

2017